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M9550117.TXT
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1995-03-04
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Document 0117
DOCN M9550117
TI Local and global structural properties of the HIV-MN V3 loop.
DT 9505
AU Catasti P; Fontenot JD; Bradbury EM; Gupta G; Theoretical Biology and
Biophysics Group, Los Alamos National; Laboratory, New Mexico 87545.
SO J Biol Chem. 1995 Feb 3;270(5):2224-32. Unique Identifier : AIDSLINE
MED/95138191
AB Studies of the feasibility of a subunit vaccine to protect against human
immunodeficiency virus (HIV) infection have principally focused on the
third variable (V3) loop. The principal neutralizing determinant (PND)
of HIV-1 is located inside the V3 loop of the surface envelope
glycoprotein, gp120. However, progress toward a PND-based vaccine has
been impeded by the amino acid sequence variability in the V3 loops of
different HIV isolates. Theoretical studies revealed that the
variability in sequence and structure of the V3 loop is confined to the
N- and C-terminal sides of the conserved GPG crest. This leaves three
regions of the V3 loop conserved both in sequence and secondary
structure. We present the results of NMR studies that test the validity
of our theoretical predictions. Structural studies are reported for the
HIV-V3 loop (HIV-MN) in the linear and cyclic (S-S-bridged) forms. For
the V3 loop sequence of the HIV-MN isolate, the three conserved
secondary structural elements are as underlined below: turns turn helix
CTRPNYNKRKRIHIGPGRAFYTTKNIIGTIROAHC Finally, the conformational
requirement of the PND in the V3 loop-antibody interaction is tested by
monitoring the monoclonal antibody binding to the HIV-MN V3 loop in the
linear and cyclic forms by enzyme-linked immunosorbent assay. The
binding data reveal that the cyclic V3 loop is a better ligand for the
monoclonal antibodies than the linear form although the latter has the
same sequence. This means that the monoclonal antibodies recognize the
PNDs as conformational epitopes.
DE Amino Acid Sequence HIV Antigens/CHEMISTRY HIV Envelope Protein
gp120/*CHEMISTRY/IMMUNOLOGY HIV-1/IMMUNOLOGY/*ULTRASTRUCTURE Models,
Molecular Molecular Sequence Data Nuclear Magnetic Resonance Protein
Structure, Secondary Solvents Support, U.S. Gov't, Non-P.H.S.
Support, U.S. Gov't, P.H.S. JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).